4cgq

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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4cgq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cgq OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4cgq RCSB], [http://www.ebi.ac.uk/pdbsum/4cgq PDBsum]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4cgq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cgq OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4cgq RCSB], [http://www.ebi.ac.uk/pdbsum/4cgq PDBsum]</span></td></tr>
</table>
</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/HS90A_HUMAN HS90A_HUMAN]] Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function.<ref>PMID:15937123</ref> <ref>PMID:11274138</ref>
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== References ==
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<references/>
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</StructureSection>
</StructureSection>

Revision as of 14:16, 25 December 2014

Full length Tah1 bound to HSP90 peptide SRMEEVD

4cgq, resolution 2.00Å

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